Characterization of the interaction between 2′-deoxyuridine and human serum albumin

The binding of 2′-deoxyuridine to human serum albumin (HSA) was investigated by fluorescence spectroscopy in combination with molecular modeling under simulation of physiological conditions. The quenching mechanism was suggested to be static according to the fluorescence measurement. The thermodynamic parameters: enthalpy change (ΔH) and entropy change (ΔS) were calculated to be −18.87 kJ/mol and 24.00 J/(mol K) according to the Vant'Hoff equation. These data suggest that hydrophobic interactions are the predominant intermolecular forces stabilizing the complex. Experimental results are in agreement with the results obtained by molecular modeling study. In addition, the effects of common ions on the binding constants were also studied at room temperature.